title: Interaction of monomeric and dimeric kinesin with microtubules.
abstract: The binding stoichiometry of kinesin to microtubules was determined using several biochemical and biophysical approaches (chemical crosslinking, binding assays, scanning transmission electron microscopy (STEM), image reconstruction, and X-ray scattering). The results show that each tubulin dimer associates with one kinesin head, irrespective of whether kinesin occurs in a monomeric or dimeric form in solution. Moreover, these heads appear to align along the protofilament axis generating a 16 nm periodicity of successive kinesin dimers. This is consistent with a "tightrope" model of movement where the first head of the dimer provides a guiding signal for the following one.
authors.affiliation: Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, Hamburg, D-22603, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Thormählen
authors.forename: A
authors.initials: A
authors.lastname: Marx
authors.forename: S A
authors.initials: SA
authors.lastname: Müller
authors.forename: Y
authors.initials: Y
authors.lastname: Song
authors.forename: E M
authors.initials: EM
authors.lastname: Mandelkow
authors.forename: U
authors.initials: U
authors.lastname: Aebi
authors.forename: E
authors.initials: E
authors.lastname: Mandelkow
mesh_terms: D000818:Animals; D001665:Binding Sites; D049832:Decapodiformes; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation; D051381:Rats; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D014404:Tubulin; D016547:Kinesins